Types of Biomolecules

Carbohydrates
1. Glycosidic bond
  1. bond between sugar molecules
2. monosaccharides
  1. galactose
  2. glucose
  3. fructose
  4. simple sugars (most common glucose) often ending with the suffix -ose
    1. aldose: has an aldehyde
    2. ketose: has a ketone
3. disaccharides
  1. lactose
  2. sucrose
  3. maltose
4. polysaccharides
  1. starch
    1. amylose
    2. amylopectin
      1. branched
  2. glycogen
    1. storage form of glucose usually in the liver and muscles of humans/vertebates
      1. whenever blood glucose levels decrease, glycogen is broken down to release glucose
  3. cellulose
    1. most abundant biopolymer
    2. cell wall of plants and wood
    3. cannot be digested by humans, only by some herbivores due to protists
    4. alternating positions of glycosidic bonds, need enzyme cellulase to be broken down
  4. chitin
    1. major component of arthropod exoskeletons and fungal cell walls
    2. N-acetyl-β-d-glucosamine
  5. short term energy storage and structural molecules
5. n(CH2O)
6. BENEFITS
  1. immediate source of energy (4.3 Kcal)
  2. insoluble part (fiber) helps bowel movement and remove excess cholesterol
Lipids
1. Ester bond
  1. bond between glycerol and fatty acid
2. insoluble in water and contain CHO (just lower number than carbs)
  1. long term energy storage, insulation, structural and protection
    1. BENEFITS
      1. essential fats
        help reduce the risk of heart attacks, reduce triglyceride levels in the blood, lower blood pressure and prevent thrombosis by inhibiting blood clotting.
        Omega-6
        Omega-3
      2. many vitamins are fat soluble
        A, D, E, K
3. fatty acids
4. waxes
  1. long chain fatty acids bond with alcohol
    1. solid at normal temperature due to high melting point
  2. prevents water loss and helps protection
5. steroids
  1. hydrocarbons with the carbons arranged in a set of 4 linked rings
  2. cholesterol
  3. hormones
6. phospholipids
  1. main component of cell membrane
  2. glycerol with 2 fatty acids attached and a phosphate head
    1. hydrophilic head and hydrophobic tail
7. triglycerides
  1. fats
    1. solid at room temperature and come from animals
      1. saturated
        more hydrogen atoms
        straight chains
  2. oils
    1. liquid at room temperature and come from plants
      1. unsaturated
        have double bonds with carbon
        crooked chains
Proteins
1. Peptide bond
  1. bonds between amino acids
    1. carboxyl group + amino acid combine to relase water
      1. chain of amino acids
        polypeptide
2. amino acids
  1. monomers that make up proteins
    1. has a central carbon atom, bonded to amino group (and R), carboxyl group, and hydrogen atom
      1. the side chain (R) determines if acidic, basic, polar, or non-polar
        sequence and number of amino acids determine protein shape and function
  2. 20 types of amino acids
    1. 10 essential amino acids
3. consists of 4 elements: Carbon, Oxygen, Hydrogen and Nitrogen with some proteins having Sulfur
  1. protein refers to a polypeptide or polypeptides that have combined together
    1. BENEFITS
      1. the most important type of macromolecule
        support
        collagen in skin, keratin in hair, crystallin in eye
        enzymes
        all metabolic transformations are done by enzynes
        transport
        oxygen in the blood is carried by hemoglobin
        nutrition
        insulin, egg yolk, contractile, antibodies
4. organized by levels of increasing complexity
  1. primary
    1. unique sequence of amino acids in a polypeptide chain
  2. secondary
    1. local folding of polypeptide in some regions
      1. a-helix
        due to hydrogen bonds that form between the O and CO and another four amino acids farther along the chain
        twirling figure
      2. b-pleated sheet
        pleats are formed by hydrogen bonding with atoms on backbone of chain
        parallel and antiparallel pleated segments
        folded paper figure
  3. tertiary
    1. interactions among R-groups
      1. Interaction between cysteine side chains forms disulfide linkages in the presence of oxygen (covalent bonding).
    2. hydrophobic interactions
      1. hydrophobic R groups of non-polarity lay interior whereas hydrophilic lay outside
  4. quarternary
    1. weak interactions of subunits
      1. some proteins are formed from several polypeptides or more than one amino acid chain
Nucleic Acids
1. Phosphate ester bond and hydrogen bond
  1. bond between phosphate and pentose sugar + bond between nitrogenous bases
2. nucleotides
3. organic compounds composed of a pentose sugar, nitrogenous base, and a phosphate group
  1. pentose sugars
    1. deoxyribose
    2. ribose
  2. nitrogenous bases
    1. adenine
    2. cytosine
    3. guanine
    4. thymine
    5. uracil

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	Criado por Julia David mais de 7 anos atrás